Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1WDM

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
A	0004300	molecular_function	enoyl-CoA hydratase activity
A	0005515	molecular_function	protein binding
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0008692	molecular_function	3-hydroxybutyryl-CoA epimerase activity
A	0009062	biological_process	fatty acid catabolic process
A	0016042	biological_process	lipid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016509	molecular_function	long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
A	0036125	cellular_component	fatty acid beta-oxidation multienzyme complex
A	0070403	molecular_function	NAD+ binding
B	0003824	molecular_function	catalytic activity
B	0003857	molecular_function	(3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B	0004165	molecular_function	delta(3)-delta(2)-enoyl-CoA isomerase activity
B	0004300	molecular_function	enoyl-CoA hydratase activity
B	0005515	molecular_function	protein binding
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0008692	molecular_function	3-hydroxybutyryl-CoA epimerase activity
B	0009062	biological_process	fatty acid catabolic process
B	0016042	biological_process	lipid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016509	molecular_function	long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0018812	molecular_function	3-hydroxyacyl-CoA dehydratase activity
B	0036125	cellular_component	fatty acid beta-oxidation multienzyme complex
B	0070403	molecular_function	NAD+ binding
C	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0010124	biological_process	phenylacetate catabolic process
C	0016042	biological_process	lipid catabolic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0044281	biological_process	small molecule metabolic process
D	0003988	molecular_function	acetyl-CoA C-acyltransferase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0010124	biological_process	phenylacetate catabolic process
D	0016042	biological_process	lipid catabolic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0044281	biological_process	small molecule metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 716

Chain	Residue
A	HIS550
A	ASP573
D	GLU266
D	VAL391

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACO A 1002

Chain	Residue
A	PRO534
A	MET535
A	TYR660
A	GLY661
A	GLY663
A	LEU666
A	LYS142
A	ASP297
A	MET459
A	ASN501
A	LEU504

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ACO C 3001

Chain	Residue
C	CYS95
C	MET130
C	MET151
C	HIS177
C	THR218
C	LEU226
C	PHE230
C	SER243
C	ILE245
C	MET284
C	ASN312
C	ALA314
C	PHE315
C	HIS347
C	CYS377

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACO D 4001

Chain	Residue
D	CYS95
D	MET130
D	MET151
D	HIS177
D	THR218
D	LEU223
D	LEU226
D	MET284
D	ASN312
D	ALA314
D	HIS347
D	CYS377

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NAD A 1001

Chain	Residue
A	GLY321
A	ALA322
A	ILE324
A	MET325
A	ASP344
A	ILE345
A	VAL401
A	GLU403
A	LYS408
A	VAL411
A	ASN428
A	SER430
A	ASN454

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE NAD B 2001

Chain	Residue
B	ILE324
B	MET325
B	ASP344
B	ILE345
B	ALA400
B	VAL401
B	GLU403
B	LYS408
B	VAL411
B	ASN428
B	SER430
B	ASN454

Functional Information from PROSITE/UniProt

site_id	PS00067
Number of Residues	25
Details	3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DcpGFLvNRvlfPYFggfak.LVsaG

Chain	Residue	Details
A	ASP494-GLY518

site_id	PS00098
Number of Residues	19
Details	THIOLASE_1 Thiolases acyl-enzyme intermediate signature. VSRlCGSSMsALhtaaqaI

Chain	Residue	Details
C	VAL91-ILE109

site_id	PS00099
Number of Residues	14
Details	THIOLASE_3 Thiolases active site. GLSTMCIGlGqGiA

Chain	Residue	Details
C	GLY372-ALA385

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAaINGialGGGlemcLaADF

Chain	Residue	Details
A	VAL107-PHE127

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pk.GGtVTAGTS

Chain	Residue	Details
C	PRO232-SER242

site_id	PS00737
Number of Residues	17
Details	THIOLASE_2 Thiolases signature 2. NlhGGaIAlGHPfGcSG

Chain	Residue	Details
C	ASN337-GLY353

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	378
Details	Region: {"description":"Enoyl-CoA hydratase/isomerase","evidences":[{"source":"HAMAP-Rule","id":"MF_01621","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"For 3-hydroxyacyl-CoA dehydrogenase activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01621","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15229654","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_01621","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01620","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01620","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
C	HIS347
C	CYS377
C	CYS95
C	GLY379

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
B	GLU140
B	GLY148

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
A	GLU120
A	GLU140
A	GLY117

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
B	GLU120
B	GLU140
B	GLY117

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
D	HIS347
D	CYS377
D	CYS95
D	GLY379

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
A	GLU120
A	GLU140
A	GLY117
A	ALA69

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
B	GLU120
B	GLU140
B	GLY117
B	ALA69

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
C	HIS347
C	CYS377

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
D	HIS347
D	CYS377

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
A	HIS451
A	SER430
A	ASN501

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
B	HIS451
B	SER430
B	ASN501

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1afw

Chain	Residue	Details
A	GLU140
A	GLY148

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)